Subcellular partitioning of transcription factors during osteoblast differentiation: Developmental association of the AML/CBFα/PEBP2α-related transcription factor-NMP-2 with the nuclear matrix

Lindenmuth, Danielle M.; Wijnen, André J. van; Hiebert, Scott W.; Stein, Janet L.; Lian, Jane B.; Stein, Gary S.

doi:10.1002/(sici)1097-4644(19970701)66:1<123::aid-jcb13>3.0.co;2-k

Cited by 31 publications

(7 citation statements)

References 38 publications

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“…Association of genes and cognate factors with the nuclear matrix may support the formation and/or activities of nuclear domains that facilitate transcriptional control (Guo et al, 1995;Merriman et al, 1995;Nickerson et al, 1995;Berezney et al, 1996;Chen et al, 1996;Nardozza et al, 1996;Stein et al, 1996;Alvarez et al, 1997;Davie, 1997;Grande et al, 1997;Jackson, 1997;Lindenmuth et al, 1997). Results from our laboratory indicate that the association of Runx transcription factors with the nuclear matrix is obligatory for activity (Zeng et al, 1998;Choi et al, 2001).…”

Section: Properties Of Transcriptionally Active Subnuclear Compartmentsmentioning

confidence: 58%

Runx2 control of organization, assembly and activity of the regulatory machinery for skeletal gene expression

et al. 2004

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We present an overview of Runx involvement in regulatory mechanisms that are requisite for fidelity of bone cell growth and differentiation, as well as for skeletal homeostasis and the structural and functional integrity of skeletal tissue. Runx-mediated control is addressed from the perspective of support for biological parameters of skeletal gene expression. We review recent findings that are consistent with an active role for Runx proteins as scaffolds for integration, organization and combinatorial assembly of nucleic acids and regulatory factors within the three-dimensional context of nuclear architecture.

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Section: Properties Of Transcriptionally Active Subnuclear Compartmentsmentioning

confidence: 58%

Runx2 control of organization, assembly and activity of the regulatory machinery for skeletal gene expression

et al. 2004

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“…The interaction of B23 with YY1 might mediate some of the changes in YY1 distribution we have observed. The compartmentalization of YY1 in the cell or even within the nucleus may also reflect different regulatory functions of YY1 in gene expression (Lindenmuth et al, 1997;Bushmeyer and Atchison, 1998;McNeil et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

The Yin Yang-1 (YY1) protein undergoes a DNA-replication-associated switch in localization from the cytoplasm to the nucleus at the onset of S phase

Palko

Bass

Beyrouthy

et al. 2004

Journal of Cell Science

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The essential Yin Yang-1 gene (YY1) encodes a ubiquitous, conserved, multifunctional zinc-finger transcription factor in animals. The YY1 protein regulates initiation, activation, or repression of transcription from a variety of genes required for cell growth, development, differentiation, or tumor suppression, as well as from genes in some retroviruses and DNA viruses. Among the specific functions attributed to YY1 is a role in cell-cycle-specific upregulation of the replication-dependent histone genes. The YY1 protein binds to the histone alpha element, a regulatory sequence found in all replication-dependent histone genes. We therefore examined the abundance, DNA-binding activity and localization of the YY1 protein throughout the cell cycle in unperturbed, shake-off-synchronized Chinese hamster ovary and HeLa cells. We found that, whereas the DNA-binding activity of YY1 increased dramatically early in S phase, the YY1 mRNA and protein levels did not. YY1 changed subcellular distribution patterns during the cell cycle, from mainly cytoplasmic at G1 to mainly nuclear at early and middle S phase, then back to primarily cytoplasmic later in S phase. Nuclear accumulation of YY1 near the G1/S boundary coincided with both an increase in YY1 DNA-binding activity and the coordinate up-regulation of the replication-dependent histone genes. The DNA synthesis inhibitor aphidicolin caused a nearly complete loss of nuclear YY1, whereas addition of caffeine or 2-aminopurine to aphidicolin-treated cells restored both DNA synthesis and YY1 localization in the nucleus. These findings reveal a mechanism by which YY1 localization is coupled to DNA synthesis and responsive to cell-cycle signaling pathways. Taken together, our results provide insight into how YY1 might participate in the cell-cycle control over a variety of nuclear events required for cell division and proliferation.

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“…To that end, HeLa cell nuclear proteins were resolved into soluble (Fig. 3B, lanes 1 and 2) and insoluble (lanes 3 and 4) fractions, which were subjected to SDS-PAGE followed by Western blotting for BLM (upper panel), hp150 (middle panel), or SP1 (lower panel), the last of which was used as a loading control (28). Interestingly, the amount of both BLM and hp150 increased, although to different extents, in the insoluble (lane 4), but not the soluble (lane 2) fraction of nuclear proteins after HU treatment of HeLa cells.…”

Section: Methodsmentioning

confidence: 99%

Physical and Functional Interaction between the Bloom's Syndrome Gene Product and the Largest Subunit of Chromatin Assembly Factor 1

Jiao

Bachrati

Pedrazzi³

et al. 2004

Molecular and Cellular Biology

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Bloom's syndrome (BS) is a genomic instability disorder characterized by cancer susceptibility. The protein defective in BS, BLM, belongs to the RecQ family of DNA helicases. In this study, we found that BLM interacts with hp150, the largest subunit of chromatin assembly factor 1 (CAF-1), in vitro and in vivo. Colocalization of a proportion of the cellular complement of these two proteins is found at specific nuclear foci coinciding with sites of DNA synthesis in the S phase. This colocalization increases in the presence of agents that damage DNA or inhibit DNA replication. In support of a functional interaction between BLM and CAF-1, we show that BLM inhibits CAF-1-mediated chromatin assembly during DNA repair in vitro. Although CAF-1 activity is not altered in BLM-deficient cells, the absence of BLM does impair the ability of CAF-1 to be mobilized within the nucleus in response to hydroxyurea treatment. Our results provide the first link between BLM and chromatin assembly coupled to DNA repair and suggest that BLM and CAF-1 function in a coordinated way to promote survival in response to DNA damage and/or replication blockade.Bloom's syndrome (BS) is a rare recessive genetic disorder associated with cancer predisposition, immunodeficiency, proportional dwarfism, and a sunlight-induced facial erythema (16). Cells from BS patients display genomic instability, including an excessive number of locus-specific mutations as well as a high frequency of microscopically visible chromatid gaps, rearrangements, breaks, and sister chromatid exchanges (40). BS cells are not defective in the known DNA repair pathways (14, 26, 38) but show a retarded rate of nascent DNA chain elongation (18) and accumulate abnormal replication intermediates (29). The gene mutated in BS encodes a DNA helicase (BLM) belonging to the RecQ family (12). Recombinant BLM exhibits ATP-dependent 3Ј-5Ј DNA helicase activity (22). Immunolocalization studies have shown that BLM is found mainly in the nucleus at discrete foci (shown to coincide with promyelocytic leukemia protein (PML) bodies) (21, 35) and in nucleoli during S phase (55).Recently, much attention has been paid to the characterization of proteins that associate with the RecQ family of DNA helicases in order to understand their exact roles in the maintenance of genome stability in human cells (19,34). BLM has been reported to interact with several proteins, including replication protein A (RPA), a DNA binding protein that plays essential roles during DNA replication, repair, and recombination (8); topoisomerase III␣, a protein that, together with BLM, can resolve intermediates that arise during homologous recombinational repair (53, 54); BRCA1, a protein required for efficient homologous recombination and which acts as a signal processor for DNA damage responses (50); RAD51 and RAD51L3, proteins required for DNA strand invasion and exchange during homologous recombination (6, 7, 52); p53, a tumor suppressor implicated in S-phase processes, DNA repair, and homologous recombination (11, 41, 49...

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Subcellular partitioning of transcription factors during osteoblast differentiation: Developmental association of the AML/CBFα/PEBP2α-related transcription factor-NMP-2 with the nuclear matrix

Cited by 31 publications

References 38 publications

Runx2 control of organization, assembly and activity of the regulatory machinery for skeletal gene expression

Runx2 control of organization, assembly and activity of the regulatory machinery for skeletal gene expression

The Yin Yang-1 (YY1) protein undergoes a DNA-replication-associated switch in localization from the cytoplasm to the nucleus at the onset of S phase

Physical and Functional Interaction between the Bloom's Syndrome Gene Product and the Largest Subunit of Chromatin Assembly Factor 1

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